Identification and characterization of the zosA gene involved in copper uptake in Bacillus subtilis 168. Issue 3 (3rd March 2016)

• Record Type: Journal Article
• Authors: Fukuhara, Takahiro; Kobayashi, Kazuo; Kanayama, Yousuke; Enomoto, Shu-ichi; Kondo, Taeko; Tsunekawa, Naoki; Nemoto, Michiko; Ogasawara, Naotake; Inagaki, Kenji; Tamura, Takashi
• Is Part Of: Bioscience, biotechnology, and biochemistry. Volume 80:Issue 3(2016)
• Page Start: 600
• Page End: 609
• Publication Date: 2016-03-03
• Subjects: Bacillus subtilis 168 -- dl-penicillamine -- zosA -- Cu-uptake ATPase -- molecular dynamics simulation; Biotechnology -- Periodicals; Biochemistry -- Periodicals; 660.6
• DOI: 10.1080/09168451.2015.1107462
• Languages: English
• ISSNs: 0916-8451

Abstract

Abstract: dl -Penicillamine, a copper-specific metal chelator, remarkably suppressed the growth of Bacillus subtilis 168 when added to a synthetic medium under Cu 2+ limitation. DNA microarray and screening of 2, 602 knockout mutants showed that the zosA gene was de-repressed in the presence of 0.1% dl -penicillamine, and that the zosA mutant was sensitive to dl -penicillamine medium. The zosA mutant delayed the growth under Cu-limitation even without the chelator, and the sensitivity to dl -penicillamine was reversed by induction using 0.3 mM IPTG and the Pspac promoter inserted directly upstream of the zosA gene. Furthermore, the zosA mutant showed elevated tolerance of excessive Cu 2+ but not of excessive Zn 2+ added to LB and synthetic media. Homology modeling of the ZosA protein suggested that the protein can fold itself into essential domains for constituting a metal transporting ATPase. Our study suggests that zosA is a candidate gene involved in copper uptake. Graphical abstract: : Modeling of ZosA protein by molecular dynamics simulation.